| Type | Description |
|---|---|
| Definition | oxysterol-binding protein OSH6 |
| Date | Results | Publications |
|---|---|---|
| 2020-01-04 11:31:00 | Data show that oxysterol-binding protein OSH6 (Osh6p) reduces its avidity for anionic membranes once it captures phosphatidylserine (PS) or phosphatidylinositol-4-phosphate (PI4P), due to a molecular lid closing its lipid-binding pocket. | 31477717 |
| 2015-08-22 10:19:00 | Phosphatidylserine (PS) transporter Osh6p extracted phosphatidylinositol 4-phosphate (PI4P) and exchanged PS for PI4P between two membranes. | 26206936 |
| 2012-10-13 11:32:00 | high-copy OSH6 expression promoted vacuole fusion in nyv1Delta, and PERG6-OSH6, which downregulates ERG11 mRNA levels, also promotes vacuole fusion in nyv1Delta. | 22622083 |
| 2010-01-21 00:00:00 | data suggest that Osh6p plays a role primarily in regulating cellular sterol metabolism, possibly stero transport | 16156791 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
OSH6_YEAST
UniprotKB:
Q02201
UniParc:
UPI0000130EB7
EMBL:
X65124,
Z28228,
BK006944
EnsemblGenome:
YKR003W
KO:
sce:YKR003W
|
| Nucleutide sequences |
EMBL-CDS:
CAA46249.1,
CAA82073.1,
DAA09159.1
Gene_ORFName:
YK102
EnsemblGenome_TRS:
YKR003W_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YKR003W
RefSeq:
NP_012928.1
|
| Others |
UniRef100:
UniRef100_Q02201
UniRef90:
UniRef90_Q02201
UniRef50:
UniRef50_Q02201
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
{{protein.nucleotideVersion}}
Ensembl: {{protein.nucleotideEnsembl}} |
{{protein.proteinVersion}}
Ensembl: {{protein.proteinEnsembl}} |
{{uniprot}} , |
Definition: {{{protein.definition}}}Transcript Veriant:{{protein.transcriptVeriant}} Status: {{protein.status}} |
||||
| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
{{conservedDomain.comments == '' || conservedDomain.comments == null ? "-" : conservedDomain.comments }} |
Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
{{conservedDomain.comments == '' || conservedDomain.comments == null ? "-" : conservedDomain.comments }} |
||||
暂无数据
| 排名 | 科研单位 | 文献 |
|---|---|---|
| {{affIndex+1}} |
{{aff.value}} |
{{aff.size}} |
目前还没有研究热点单位
| 排名 | 研究人员 | 文献 |
|---|---|---|
| {{authorIndex+1}} |
{{author.value}} |
{{author.size}} |
目前还没有研究热点人员